Protamines. VII. Circular Dichroism Study of Salmine A I

G. M. Bonora 1 , F. Bertanzon 1 , V. Moretto 1  and C. Toniolo 1
  • 1 Centro di Studi sui Biopolimeri, C.N.R., Istituto di Chimica Organica, Universita’ di Padova, Via Marzolo 1, 35100 Padova, Italy

Salmine A I, one of the components of the protamine from salmon, has been purified and characterized. The conformational preferences of salmine A I have been examined as a function of pH, added salts, presence of helix-supporting solvents, and temperature, using circular dichroism. It has been found that this small basic protein adopts predominantly an unordered conformation in aqueous solution. Addition of counter-ions, in particular perchlorate, and 2-chloroethanol induces to various extents the onset of the right-handed α-helical conformation. The results are discussed in comparison with those previously reported on the three main components of clupeine, the protamine from herring, and with the published conformational predictions by various statistical methods

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A Journal of Biosciences: Zeitschrift für Naturforschung C (ZNC) is an international scientific journal for the emerging field of natural and natural-like products. ZNC publishes original research on the isolation, bio-chemical synthesis and bioactivities of natural products, their biochemistry, pharmacology, biotechnology, and biological activity and innovative developed computational methods for predicting their structure and/or function.